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P58913

- CO16A_CONPU

UniProt

P58913 - CO16A_CONPU

Protein

Delta-conotoxin PVIA

Gene
N/A
Organism
Conus purpurascens (Purple cone)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Delta-conotoxins bind to site 6 of voltage-gated sodium channels (Nav) and inhibit the inactivation process. In mice, injection of this toxin causes hyperactivity, rapid running, limb extension, and death. In fish, the peptide elicites spurts of rapid swimming, with twisted motions, quivering fins and the lockjaw extended mouth syndrome. Rigid paralysis and death are observed at higher doses. In mollusks, this peptide is inactive. Injection of this peptide together with the kappa-conotoxin PVIIA causes the sudden tetanus of prey (STOP) syndrome, which is a single, lethal "fin-pop" in envenomed fish.

    GO - Molecular functioni

    1. sodium channel inhibitor activity Source: InterPro

    GO - Biological processi

    1. pathogenesis Source: InterPro

    Keywords - Molecular functioni

    Ion channel impairing toxin, Neurotoxin, Toxin, Voltage-gated sodium channel impairing toxin

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-conotoxin PVIA
    Alternative name(s):
    Lockjaw peptide
    OrganismiConus purpurascens (Purple cone)
    Taxonomic identifieri41690 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaGastropodaCaenogastropodaHypsogastropodaNeogastropodaConoideaConidaeConus

    Organism-specific databases

    ConoServeri1563. PVIA precursor.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591T → A: No loss of activity. 1 Publication
    Mutagenesisi60 – 601F → A: Loss of biological activity. However, coinjection of this mutant protects against the wild-type conotoxin, suggesting that the mutant binds competitively to the wild-type conotoxin ligand site. Such a protective effect does not occur for all physiological targets. 1 Publication
    Mutagenesisi63 – 631I → A: Loss of activity. 1 Publication
    Mutagenesisi64 – 641K → A: No loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 4927By similarityPRO_0000034898Add
    BLAST
    Peptidei52 – 8029Delta-conotoxin PVIAPRO_0000034899Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 69By similarity
    Modified residuei57 – 5714-hydroxyproline1 Publication
    Disulfide bondi61 ↔ 73By similarity
    Modified residuei65 – 6514-hydroxyproline1 Publication
    Disulfide bondi68 ↔ 78By similarity
    Modified residuei80 – 801Glycine amide; in form delta-conotoxin PVIA

    Post-translational modificationi

    The difference between delta-conotoxin PVIA and [deamido]-delta-conotoxin PVIA lies in the state of amidation of Gly-80.

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues, Disulfide bond, Hydroxylation

    Expressioni

    Tissue specificityi

    Expressed by the venom duct.

    Family & Domainsi

    Domaini

    The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.By similarity
    The cysteine framework is VI/VII (C-C-CC-C-C).

    Sequence similaritiesi

    Belongs to the conotoxin O1 superfamily.Curated

    Keywords - Domaini

    Knottin, Signal

    Family and domain databases

    InterProiIPR004214. Conotoxin.
    IPR012322. Conotoxin_d-typ_CS.
    [Graphical view]
    PfamiPF02950. Conotoxin. 1 hit.
    [Graphical view]
    PROSITEiPS60005. DELTA_CONOTOXIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P58913-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLTCVMIVA VLFLTAWTFV TADDSKNGLE NHFWKARDEM KNREASKLDK   50
    KEACYAPGTF CGIKPGLCCS EFCLPGVCFG G 81
    Length:81
    Mass (Da):8,945
    Last modified:July 26, 2002 - v1
    Checksum:iACCFE9E1C65ABFEC
    GO

    Mass spectrometryi

    Molecular mass is 2997.3 Da from positions 52 - 80. 1 Publication

    Sequence databases

    PIRiA58651.

    Cross-referencesi

    Sequence databases

    PIRi A58651.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    ConoServeri 1563. PVIA precursor.

    Family and domain databases

    InterProi IPR004214. Conotoxin.
    IPR012322. Conotoxin_d-typ_CS.
    [Graphical view ]
    Pfami PF02950. Conotoxin. 1 hit.
    [Graphical view ]
    PROSITEi PS60005. DELTA_CONOTOXIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification, characterization, synthesis, and cloning of the lockjaw peptide from Conus purpurascens venom."
      Shon K.-J., Grilley M.M., Marsh M., Yoshikami D., Hall A.R., Kurz B., Gray W.R., Imperial J.S., Hillyard D.R., Olivera B.M.
      Biochemistry 34:4913-4918(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-80, SYNTHESIS OF 52-80, HYDROXYLATION AT PRO-57 AND PRO-65, MASS SPECTROMETRY.
      Tissue: Venom and Venom duct.
    2. "Strategy for rapid immobilization of prey by a fish-hunting marine snail."
      Terlau H., Shon K.-J., Grilley M.M., Stocker M., Stuehmer W., Olivera B.M.
      Nature 381:148-151(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 52-80, SYNTHESIS OF 52-80.
    3. Cited for: SYNTHESIS OF 52-80, MUTAGENESIS OF THR-59; PHE-60; ILE-63 AND LYS-64.

    Entry informationi

    Entry nameiCO16A_CONPU
    AccessioniPrimary (citable) accession number: P58913
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 26, 2002
    Last sequence update: July 26, 2002
    Last modified: October 1, 2014
    This is version 58 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3